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Bamford, Vicki, Dobbin, Paul S., Richardson, David J. 
ORCID: https://orcid.org/0000-0002-6847-1832 and Hemmings, Andrew M. ORCID: https://orcid.org/0000-0003-3053-3134
(1999)
Open conformation of a flavocytochrome c3 fumarate reductase.
Nature Structural Biology, 6 (12).
pp. 1104-1107.
ISSN 1072-8368
Abstract
Fumarate reductases and succinate dehydrogenases play central roles in the metabolism of eukaryotic and prokaryotic cells. A recent medium resolution structure of the Escherichia coli fumarate reductase (Frd) has revealed the overall organization of the membrane-bound complex. Here we present the first high resolution X-ray crystal structure of a water-soluble bacterial fumarate reductase in an open conformation. This structure reveals a mobile domain that modulates substrate access to the active site and provides new insights into the mechanism of this widespread and important family of FAD-containing respiratory proteins.
| Item Type: | Article |
|---|---|
| Additional Information: | Funding Information: We would like to acknowledge the support of the Wellcome Trust to P.S.D. and D.J.R. We are grateful also for access to the facilities of the BM14 beamline at the ESRF, the EMBL BW7B beamline at the Doris storage ring, DESY, Hamburg, and the UEA Centre for Metalloprotein Spectroscopy and Biology (CMSB). |
| Uncontrolled Keywords: | structural biology,biochemistry,genetics ,/dk/atira/pure/subjectarea/asjc/1300/1315 |
| Faculty \ School: | Faculty of Science > School of Biological Sciences |
| UEA Research Groups: | Faculty of Science > Research Groups > Organisms and the Environment Faculty of Science > Research Groups > Molecular Microbiology Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry |
| Related URLs: | |
| Depositing User: | LivePure Connector |
| Date Deposited: | 15 Jul 2022 12:30 |
| Last Modified: | 15 May 2023 00:54 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/86195 |
| DOI: | 10.1038/70039 |
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